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Date of Award


Document Type

Restricted Thesis: Campus only access

Degree Name

Bachelor of Science



First Advisor

Dr. Linda Boland


Potassium two-pore domain (K2P) channels play an important role in the regulation of the resting membrane potential and electrical signaling. Among the subfamilies of K2P, there is a lack of conservation of the C-terminal sequence, supporting the idea that the unique sensitivity of each K2P subfamily is based in the C-terminus. The TREK subfamily is activated by alkaline pH, fatty acids, membrane stretch, and phosphorylation. Previous studies have characterized regions of the C-terminus in their role of responding to these stimuli. Using Xenopus oocyte expression in conjunction with chemiluminescence techniques, we aimed to investigate the role of regions of the TREK-1 C-terminus in regulation of sensitivity to a fatty acid. Chemiluminescence assays of epitope-tagged TREK-1 C-terminal mutants suggest that the region between G308 and L332 is critical for channel expression. Whole cell recordings suggest that the proximal region of the C-terminus plays a role in activation by arachidonic acid (AA). In trying to connect these critical regions to previously-characterized regions, we are moving toward investigating the overlapping roles of AKAP scaffolding proteins and GRK phosphorylation in activation of TREK by AA.

Available for download on Saturday, November 17, 2018